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Method for Non-Covalent Immobilization of Infectious Prion Protein

Prion diseases are fatal neurodegenerative illnesses that occur in genetic, sporadic and infectious forms. From a public health perspective, prion diseases are challenging to control because infectious prions are highly resistant to environmental degradation and can potentially be transmitted by several different routes. The critical molecular event in the pathogenesis of prion diseases is the misfolding of the host-encoded prion protein (PrPC) into an infectious isoform (PrPSc).

Dartmouth scientists have now found that magnetic substrates, e.g., magnetic iron oxide substrates, non-covalently bind the infectious conformer of the prion protein, PrpSc, selectively and with high affinity. Furthermore, immobilized PrpSc serves as a competent seed for prion amplification techniques such as Protein Misfolding Cyclic Amplification (PMCA). In addition, magnetic substrates bind to PrpSc molecules from a variety of prion isolates in different animal species, but do not bind the normal conformer of the prion protein, Prpc, or the vast majority of other proteins. Therefore, in addition to diagnostic applications, immmobilization of prion proteins with magnetic substrates can be used to effectively remove infectious prion proteins from blood and/or plasma supplies, as well as in capturing infectious prion protein in vivo thereby facilitating the prevention or treatment of a prion-associated disease.

These findings are claimed in a pending patent application. We are seeking an industrial partner to further refine and market this technology. (Ref: J583)

Last Updated: 7/24/12